Journal of Agricultural and Food Chemistry · 1999 · 204 citations · 5 references
Life SciencesBiochemistryPharmacologyBiochemical PharmacologyEnzymologyFood ChemistryEnzyme InhibitionFood Effects On Oral AbsorptionCarbohydrate-based InhibitorsCarbohydrate-derived Enzyme InhibitorsEnzyme Inhibition AssaysEnzyme Inhibition By FoodEnzyme Inhibition ScreeningGastrointestinal Enzyme InhibitionGlycosidase InhibitionGlycosidase Inhibitors
The inhibitory effect of alpha-glucosidase (AGH) inhibitors against its origins (baker's yeast and rat, rabbit, and pig small intestines) was investigated. All inhibitors used in this study showed quite different inhibitory activities according to AGH origins. Voglibose, acarbose and glucono-1,5-lactone strongly inhibited mammalian AGHs, whereas no or less inhibition was observed in yeast AGH. On the contrary, (+)-catechin, a good inhibitor against yeast AGH (IC(50) = 1.3 x 10(-)(1) mM) as well as voglibose (IC(50) = 2.6 x 10(-)(2) mM), did not retard the mammalian AGH activity. Subsequent inhibition study with various food components revealed that all of foods except for green (IC(50) = 0.735 mg/mL) and oolong teas (IC(50) = 1.34 mg/mL) showed no inhibitory activity against rat AGH, whereas they inhibited yeast AGH. Consequently, the magnitude of AGH inhibition was greatly affected by its origin, and more attention relating to AGH origin would be needed to evaluate in vitro AGH inhibitory effect.
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